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FtsZ protofilaments use a hinge-opening mechanism for constrictive force generation
Ying Li1, Jen Hsin, Lingyun Zhao
1Life Sciences Institute, Zhejiang University, Hangzhou, 310058 Zhejiang, P.R. China.
Science (New York, N.Y.)
|July 27, 2013
Summary
The bacterial cell division protein FtsZ forms a Z-ring that constricts the cell membrane. Its curved structure, revealed by crystallography, explains how guanosine triphosphate hydrolysis drives cell division.
Area of Science:
- Microbiology
- Structural Biology
- Biochemistry
Background:
- FtsZ is an essential bacterial protein crucial for cell division.
- It forms the Z-ring at the division site, utilizing GTP hydrolysis for constriction.
- The precise mechanism of Z-ring-mediated constriction is not fully understood.
Purpose of the Study:
- To elucidate the structural basis of FtsZ-mediated cytokinesis.
- To investigate the conformational changes in FtsZ during its functional cycle.
Main Methods:
- X-ray crystallography was used to determine the structure of Mycobacterium tuberculosis FtsZ.
- The structure was solved for a guanosine diphosphate (GDP)-bound protofilament.
Main Results:
- The crystal structure revealed a curved conformational state of the FtsZ protofilament.
- A key longitudinal interface essential for FtsZ function was identified.
- A hydrolysis-dependent conformational switch at the T3 loop was observed, leading to subunit bending.
Conclusions:
- The protofilament curvature and subunit bending mechanism provide insight into force generation during cytokinesis.
- This structural understanding of FtsZ offers potential targets for novel antibacterial strategies.
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